Literature summary for 1.14.13.234 extracted from

Wang, P.; Bashiri, G.; Gao, X.; Sawaya, M.R.; Tang, Y.
Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis (2013), J. Am. Chem. Soc., 135, 7138-7141.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Streptomyces lividans and Escherichia coli	Streptomyces rimosus subsp. rimosus

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of OxyS in complex with oxidized flavin to 2.6 A resolution. The monomeric OxyS is comprised of three structural domains, including the FAD-binding domain (residues 1-175 and 271-389), the middle domain (residues 176-270), and the C-terminal thioredoxin-like domain (residues 390?503). The tetracycline substrate is anchored in a narrow hydrophobic cleft at the interface between the FAD-binding and the middle domains	Streptomyces rimosus subsp. rimosus

Crystallization (Comment)

Organism

structure of OxyS in complex with oxidized flavin to 2.6 A resolution. The monomeric OxyS is comprised of three structural domains, including the FAD-binding domain (residues 1-175 and 271-389), the middle domain (residues 176-270), and the C-terminal thioredoxin-like domain (residues 390?503). The tetracycline substrate is anchored in a narrow hydrophobic cleft at the interface between the FAD-binding and the middle domains

Streptomyces rimosus subsp. rimosus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces rimosus subsp. rimosus	L8EUQ6	bifunctional enzyme, catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38) and performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, reaction of EC 1.14.13.234	-
Streptomyces rimosus subsp. rimosus ATCC 10970	L8EUQ6	bifunctional enzyme, catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (EC 1.14.13.38) and performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, reaction of EC 1.14.13.234	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5a,11a-dehydrotetracycline + NADPH + H+ + O2	-	Streptomyces rimosus subsp. rimosus	5a,11a-dehydrooxytetracycline + NADP+ + H2O	-	?
5a,11a-dehydrotetracycline + NADPH + H+ + O2	-	Streptomyces rimosus subsp. rimosus ATCC 10970	5a,11a-dehydrooxytetracycline + NADP+ + H2O	-	?

Synonyms

Synonyms	Comment	Organism
oxyS	-	Streptomyces rimosus subsp. rimosus

General Information

General Information	Comment	Organism
physiological function	OxyS catalyzes two sequential hydroxylations at C6 and C5 positions of anhydrotetracycline with opposite stereochemistry. OxyS and reductase OxyR are sufficient to produce the mature tetracycline scaffold, i.e. the complete conversion of anhydrotetracycline to oxytetracycline and tetracycline. OxyS catalyzes the stereospecific hydroxylation of anhydrotetracycline at C-6 (reaction of EC 1.14.13.38). If the released product is captured by EC 1.3.98.4, 5a,11a-dehydrotetracycline dehydrogenase (OxyR), it is reduced to tetracycline. However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C-5, producing 5a,11a-dehydrooxytetracycline, which, following the action of OxyR, becomes oxytetracycline	Streptomyces rimosus subsp. rimosus